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Q03529

- SCS7_YEAST

UniProt

Q03529 - SCS7_YEAST

Protein

Ceramide very long chain fatty acid hydroxylase SCS7

Gene

SCS7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3.6 Publications

    Cofactori

    Iron.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi72 – 721Iron (heme axial ligand)PROSITE-ProRule annotation

    GO - Molecular functioni

    1. fatty acid alpha-hydroxylase activity Source: SGD
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. inositolphosphoceramide metabolic process Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13537.
    YEAST:YMR272C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ceramide very long chain fatty acid hydroxylase SCS7 (EC:1.-.-.-)
    Short name:
    Ceramide VLCFA hydroxylase SCS7
    Alternative name(s):
    Suppressor of calcium sensitivity 7
    Gene namesi
    Name:SCS7
    Synonyms:FAH1
    Ordered Locus Names:YMR272C
    ORF Names:YM8156.14C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR272c.
    SGDiS000004885. SCS7.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Ceramide very long chain fatty acid hydroxylase SCS7PRO_0000185407Add
    BLAST

    Proteomic databases

    MaxQBiQ03529.
    PaxDbiQ03529.
    PeptideAtlasiQ03529.

    Expressioni

    Gene expression databases

    GenevestigatoriQ03529.

    Interactioni

    Protein-protein interaction databases

    BioGridi35451. 525 interactions.
    IntActiQ03529. 34 interactions.
    MINTiMINT-4498866.
    STRINGi4932.YMR272C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03529.
    SMRiQ03529. Positions 13-85.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 196196CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini218 – 2225LumenalSequence Analysis
    Topological domaini244 – 29754CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini319 – 35234LumenalSequence AnalysisAdd
    BLAST
    Topological domaini374 – 38411CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei197 – 21721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei223 – 24321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei298 – 31821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei353 – 37321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 9082Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The histidine box domains may contain the active site and/or be involved in metal ion binding.

    Sequence similaritiesi

    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3000.
    GeneTreeiENSGT00390000002142.
    HOGENOMiHOG000023981.
    OMAiMKAHHVK.
    OrthoDBiEOG7RNK98.

    Family and domain databases

    Gene3Di3.10.120.10. 1 hit.
    InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR006694. Fatty_acid_hydroxylase.
    IPR014430. Ino-phos-ceramide-B_Hydrxlase.
    [Graphical view]
    PfamiPF00173. Cyt-b5. 1 hit.
    PF04116. FA_hydroxylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
    PRINTSiPR00363. CYTOCHROMEB5.
    SUPFAMiSSF55856. SSF55856. 1 hit.
    PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q03529-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE    50
    SILDYAGKDI TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT 100
    NKNHKVEVQL SADGTEFDST TFVKELPAEE KLSIATDYSN DYKKHKFLDL 150
    NRPLLMQILR SDFKKDFYVD QIHRPRHYGK GSAPLFGNFL EPLTKTAWWV 200
    VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE YGLHRFLFHF 250
    DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF 300
    ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY 350
    KNYQLGFGVT SWFWDEVFGT YLGPDAPLSK MKYE 384
    Length:384
    Mass (Da):44,881
    Last modified:November 1, 1997 - v1
    Checksum:iDF4BA5F2E0EA2218
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49260 Genomic DNA. Translation: CAA89255.1.
    AY693150 Genomic DNA. Translation: AAT93169.1.
    BK006946 Genomic DNA. Translation: DAA10172.1.
    PIRiS54484.
    RefSeqiNP_013999.1. NM_001182779.1.

    Genome annotation databases

    EnsemblFungiiYMR272C; YMR272C; YMR272C.
    GeneIDi855315.
    KEGGisce:YMR272C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49260 Genomic DNA. Translation: CAA89255.1 .
    AY693150 Genomic DNA. Translation: AAT93169.1 .
    BK006946 Genomic DNA. Translation: DAA10172.1 .
    PIRi S54484.
    RefSeqi NP_013999.1. NM_001182779.1.

    3D structure databases

    ProteinModelPortali Q03529.
    SMRi Q03529. Positions 13-85.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35451. 525 interactions.
    IntActi Q03529. 34 interactions.
    MINTi MINT-4498866.
    STRINGi 4932.YMR272C.

    Proteomic databases

    MaxQBi Q03529.
    PaxDbi Q03529.
    PeptideAtlasi Q03529.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR272C ; YMR272C ; YMR272C .
    GeneIDi 855315.
    KEGGi sce:YMR272C.

    Organism-specific databases

    CYGDi YMR272c.
    SGDi S000004885. SCS7.

    Phylogenomic databases

    eggNOGi COG3000.
    GeneTreei ENSGT00390000002142.
    HOGENOMi HOG000023981.
    OMAi MKAHHVK.
    OrthoDBi EOG7RNK98.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13537.
    YEAST:YMR272C-MONOMER.

    Miscellaneous databases

    NextBioi 979008.
    PROi Q03529.

    Gene expression databases

    Genevestigatori Q03529.

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR006694. Fatty_acid_hydroxylase.
    IPR014430. Ino-phos-ceramide-B_Hydrxlase.
    [Graphical view ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF04116. FA_hydroxylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005149. IPC-B_HD. 1 hit.
    PRINTSi PR00363. CYTOCHROMEB5.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids."
      Mitchell A.G., Martin C.E.
      J. Biol. Chem. 272:28281-28288(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p."
      Haak D., Gable K., Beeler T., Dunn T.
      J. Biol. Chem. 272:29704-29710(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain."
      Dunn T.M., Haak D., Monaghan E., Beeler T.J.
      Yeast 14:311-321(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces cerevisiae."
      Swain E., Baudry K., Stukey J., McDonough V., Germann M., Nickels J.T. Jr.
      J. Biol. Chem. 277:26177-26184(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.
    11. "Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae."
      Guan X.L., Wenk M.R.
      Yeast 23:465-477(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro."
      Bosson R., Guillas I., Vionnet C., Roubaty C., Conzelmann A.
      Eukaryot. Cell 8:306-314(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSCS7_YEAST
    AccessioniPrimary (citable) accession number: Q03529
    Secondary accession number(s): D6W098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3290 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3